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. Author manuscript; available in PMC: 2014 Sep 19.
Published in final edited form as: Chem Biol. 2013 Sep 5;20(9):1107–1115. doi: 10.1016/j.chembiol.2013.07.015

Figure 3.

Figure 3

Stereoview of the superposition of the acyl-enzyme intermediate in OXA-23 (green), OXA-24 (magenta) and OXA-1 (white). The two hydrophobic residues which interact with the 6a-hydroxyethyl moiety of the intermediate are shown at upper right (Leu166 for OXA-23 and Leu161 for OXA-1) and lower right (Val128 for OXA-23). The difference in conformation of the leucine residue can be seen. The residues which constitute the tunnel-like structure in the OXA enzymes are indicated for OXA-23 (Phe110 and Met221). See also Figure S3 and Table S1.